The PDLIM4 antibody is designed to detect the protein PDZ and LIM domain-containing protein 4 (PDLIM4), a member of the PDZ-LIM family involved in cytoskeletal organization, signal transduction, and transcriptional regulation. PDLIM4. also known as RIL or CLP36. contains a PDZ domain for protein-protein interactions and LIM domains for binding to actin-associated proteins. It acts as an adaptor molecule, linking cytoskeletal components to signaling pathways, and may regulate cell adhesion, migration, and differentiation by modulating transcription factors like NF-κB or TGF-β effectors.
Research highlights PDLIM4's dual roles in cancer. It can act as a tumor suppressor in certain contexts (e.g., prostate and breast cancers) by inhibiting oncogenic pathways, while showing oncogenic properties in others (e.g., lung adenocarcinoma). Dysregulated PDLIM4 expression correlates with tumor progression and metastasis, making it a potential biomarker. The antibody is widely used in techniques like Western blot, immunohistochemistry, and immunofluorescence to analyze its expression patterns, subcellular localization (cytoplasmic/nuclear), and interactions in normal vs. diseased tissues.
Commercially available PDLIM4 antibodies are typically raised against specific epitopes (e.g., human PDLIM4 amino acids 100-200) and validated for cross-reactivity across species (human, mouse, rat). Proper validation using knockout controls is critical due to potential cross-reactivity with other PDZ-LIM family members. Its applications span basic research in cell signaling and cancer biology to clinical studies exploring diagnostic or therapeutic targets.